Results 141 to 150 of about 39,254 (300)

In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols

open access: yesFEBS Open Bio, EarlyView.
Tyrosinase from Ralstonia pseudosolanacearum is a promising biocatalyst for producing valuable catechols from monophenol substrates. This tyrosinase is uniquely suited to this due to its high monophenolase : diphenolase ratio. We combined in silico docking and in vivo kinetic characterisation of this tyrosinase with 11 industrially relevant monophenols,
James Britton   +6 more
wiley   +1 more source

Aspartic proteinases in disease: A structural perspective

open access: yes, 2002
The aspartic proteinases are a family of enzymes involved in a number of important biological processes. In animals the enzyme renin has a hypertensive action through its role in the renin-angiotensin system.
Cooper, J.B.
core   +1 more source

Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies

open access: yesFEBS Open Bio, EarlyView.
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen   +5 more
wiley   +1 more source

proteinase

open access: yes
Citation: 'proteinase' in the IUPAC Compendium of Chemical Terminology, 5th ed.; International Union of Pure and Applied Chemistry; 2025. Online version 5.0.0, 2025. 10.1351/goldbook.12719 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
openaire   +1 more source

Protocol for quantifying miRNA trafficking across the endosomal membrane

open access: yesFEBS Open Bio, EarlyView.
An in vitro protocol measures miRNA uptake into endosomes isolated from mammalian cell extracts, which are free of subcellular contaminants. Performed at 37 °C in the presence of ATP, it ensures the import of single‐stranded miRNA into the endosomal lumen.
Syamantak Ghosh   +2 more
wiley   +1 more source

Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum

open access: yesFEBS Open Bio, EarlyView.
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey   +4 more
wiley   +1 more source

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